7jvw - Revision history

OCA at 15:12, 18 October 2023

OCA — Wed, 18 Oct 2023 15:12:26 GMT

←Older revision		Revision as of 15:12, 18 October 2023
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	<StructureSection load='7jvw' size='340' side='right'caption='[[7jvw]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='7jvw' size='340' side='right'caption='[[7jvw]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7jvw]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=7JVW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7jvw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JVW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3N:4-(DIMETHYLAMINO)-N-[7-(HYDROXYAMINO)-7-OXOHEPTYL]BENZAMIDE'>B3N</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4030178Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC8, HDACL1, CDA07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3N:4-(DIMETHYLAMINO)-N-[7-(HYDROXYAMINO)-7-OXOHEPTYL]BENZAMIDE'>B3N</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvw OCA], [https://pdbe.org/7jvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jvw RCSB], [https://www.ebi.ac.uk/pdbsum/7jvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvw ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=7jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvw OCA], [~~http~~://pdbe.org/7jvw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=7jvw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/7jvw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvw ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>	+	[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 7jvw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 7jvw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone deacetylase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Christianson~~, D W~~]]	+	[[Category: Christianson DW]]
-	[[Category: Decroos, C]]	+	[[Category: Decroos C]]
-	[[Category: Lee, M]]	+	[[Category: Lee M]]
-	[[Category: Osko~~, J D~~]]	+	[[Category: Osko JD]]
-	[[Category: Porter~~, N J]]~~	+	[[Category: Porter NJ]]
-	~~[[Category: Hydrolase~~]]	+

OCA at 07:05, 30 December 2020

OCA — Wed, 30 Dec 2020 07:05:59 GMT

←Older revision		Revision as of 07:05, 30 December 2020
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	==Crystal structure of human histone deacetylase 8 (HDAC8) G320R mutation complexed with M344==		==Crystal structure of human histone deacetylase 8 (HDAC8) G320R mutation complexed with M344==
-	<StructureSection load='7jvw' size='340' side='right'caption='[[7jvw]]' scene=''>	+	<StructureSection load='7jvw' size='340' side='right'caption='[[7jvw]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JVW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7jvw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JVW FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvw OCA], [http://pdbe.org/7jvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jvw RCSB], [http://www.ebi.ac.uk/pdbsum/7jvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvw ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3N:4-(DIMETHYLAMINO)-N-[7-(HYDROXYAMINO)-7-OXOHEPTYL]BENZAMIDE'>B3N</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC8, HDACL1, CDA07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvw OCA], [http://pdbe.org/7jvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jvw RCSB], [http://www.ebi.ac.uk/pdbsum/7jvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvw ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cornelia de Lange Syndrome (CdLS) and associated spectrum disorders are characterized by one or more congenital anomalies including distinctive facial features, upper limb abnormalities, intellectual disability, and other symptoms. The molecular genetic basis of CdLS is linked to defects in cohesin, a protein complex that functions in sister chromatid cohesion, chromatin organization, and transcriptional regulation. Histone deacetylase 8 (HDAC8) plays an important role in cohesin function by catalyzing the deacetylation of SMC3, which is required for efficient recycling of the cohesin complex. Missense mutations in HDAC8 have been identified in children diagnosed with CdLS spectrum disorders, and here we outline structure-function relationships for four of these mutations. Specifically, we report the 1.50 A-resolution structure of the I45T HDAC8-suberoylanilide hydroxamic acid complex, the 1.84 A-resolution structure of E66D/Y306F HDAC8 complexed with a peptide assay substrate, and the 2.40 A-resolution structure of G320R HDAC8 complexed with the inhibitor M344. Additionally, we present a computationally generated model of D176G HDAC8. These structures illuminate new structure-function relationships for HDAC8 and highlight the importance of long-range interactions in the protein scaffold that can influence catalytic function.
		+
		+	Structural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders.,Osko JD, Porter NJ, Decroos C, Lee MS, Watson PR, Raible SE, Krantz ID, Deardorff MA, Christianson DW J Struct Biol. 2020 Dec 11;213(1):107681. doi: 10.1016/j.jsb.2020.107681. PMID:33316326<ref>PMID:33316326</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7jvw" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Histone deacetylase]]
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Christianson DW]]	+	[[Category: Christianson, D W]]
-	[[Category: Decroos C]]	+	[[Category: Decroos, C]]
-	[[Category: Lee M]]	+	[[Category: Lee, M]]
-	[[Category: Osko JD]]	+	[[Category: Osko, J D]]
-	[[Category: Porter NJ]]	+	[[Category: Porter, N J]]
		+	[[Category: Hydrolase]]

OCA at 12:36, 16 December 2020

OCA — Wed, 16 Dec 2020 12:36:17 GMT

←Older revision		Revision as of 12:36, 16 December 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7jvw is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of human histone deacetylase 8 (HDAC8) G320R mutation complexed with M344==
-		+	<StructureSection load='7jvw' size='340' side='right'caption='[[7jvw]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JVW FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvw OCA], [http://pdbe.org/7jvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jvw RCSB], [http://www.ebi.ac.uk/pdbsum/7jvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvw ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Christianson DW]]
		+	[[Category: Decroos C]]
		+	[[Category: Lee M]]
		+	[[Category: Osko JD]]
		+	[[Category: Porter NJ]]

OCA: Protected "7jvw" [edit=sysop:move=sysop]

OCA — Wed, 02 Sep 2020 05:23:06 GMT

Protected "7jvw" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:23, 2 September 2020

OCA: New page: '''Unreleased structure''' The entry 7jvw is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Wed, 02 Sep 2020 05:23:04 GMT

New page: '''Unreleased structure''' The entry 7jvw is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7jvw is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]